Abstract
Abstract The kinetic and thermodynamic properties of aldolase and D-glyceraldehyde-3-phosphate dehydrogenase were studied in the presence of soluble poly(vinyl alcohol), poly(N-vinyl pyrrolidone) and poly(acrylic acid). Two kinds of aldolase preparations were found which did not differ in specific activity, but showed differences in respect of their kinetic response to polymer action. Preparation type a was more active at low concentrations of the polymers, and less active at high concentrations, than in buffer solution. In the case of type b preparation the polymer concentration dependence was detectable only in solutions containing poly(acrylic acid); poly (vinyl alcohol) had no effect in the concentration range studied, whereas poly(N-vinyl pyrrolidone) caused inhibition rather than activation of the enzyme. However, the thermodynamic data indicate that the polymer interacts with the enzyme even in those cases where kinetic effects are absent. Alteration of the steric structure of poly(vinyl alcohol) by intramolecular crosslinks caused qualitative changes in its effect on aldolase activity. In the case of D-glyceraldehyde-3-phosphate dehydrogenase, a dissociable tetramer, the kinetic consequences of polymer action depend on the oligomeric state of the enzyme. It appears that the above non-specific enzyme—macromolecule interactions are considerably influenced by the colloidal state of both interacting partners.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
